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1.
Proc Natl Acad Sci U S A ; 115(50): 12728-12732, 2018 12 11.
Artigo em Inglês | MEDLINE | ID: mdl-30478037

RESUMO

Bioluminescence is found across the entire tree of life, conferring a spectacular set of visually oriented functions from attracting mates to scaring off predators. Half a dozen different luciferins, molecules that emit light when enzymatically oxidized, are known. However, just one biochemical pathway for luciferin biosynthesis has been described in full, which is found only in bacteria. Here, we report identification of the fungal luciferase and three other key enzymes that together form the biosynthetic cycle of the fungal luciferin from caffeic acid, a simple and widespread metabolite. Introduction of the identified genes into the genome of the yeast Pichia pastoris along with caffeic acid biosynthesis genes resulted in a strain that is autoluminescent in standard media. We analyzed evolution of the enzymes of the luciferin biosynthesis cycle and found that fungal bioluminescence emerged through a series of events that included two independent gene duplications. The retention of the duplicated enzymes of the luciferin pathway in nonluminescent fungi shows that the gene duplication was followed by functional sequence divergence of enzymes of at least one gene in the biosynthetic pathway and suggests that the evolution of fungal bioluminescence proceeded through several closely related stepping stone nonluminescent biochemical reactions with adaptive roles. The availability of a complete eukaryotic luciferin biosynthesis pathway provides several applications in biomedicine and bioengineering.


Assuntos
Fungos/genética , Proteínas Luminescentes/genética , Sequência de Aminoácidos , Animais , Vias Biossintéticas/genética , Ácidos Cafeicos , Linhagem Celular , Linhagem Celular Tumoral , Feminino , Duplicação Gênica/genética , Células HEK293 , Células HeLa , Humanos , Camundongos , Camundongos Endogâmicos BALB C , Alinhamento de Sequência , Xenopus laevis
2.
Photochem Photobiol ; 93(2): 416-428, 2017 03.
Artigo em Inglês | MEDLINE | ID: mdl-28063169

RESUMO

Even though bioluminescent oligochaetes rarely catch people's eyes due to their secretive lifestyle, glowing earthworms sighting reports have come from different areas on all continents except Antarctica. A major breakthrough in the research of earthworm bioluminescence occurred in the 1960s with the studies of the North American Diplocardia longa. Comparative studies conducted on 13 earthworm species belonging to six genera showed that N-isovaleryl-3-aminopropanal (Diplocardia luciferin) is the common substrate for bioluminescence in all examined species, while luciferases appeared to be responsible for the color of bioluminescence. The second momentous change in the situation has occurred with the discovery in Siberia (Russia) of two unknown luminous enchytraeids. The two bioluminescent systems belong to different types, have different spectral characteristics and localization, and different temperature and pH optima. They are unique, and this fact is confirmed by the negative results of all possible cross-reactions. The bioluminescent system of Henlea sp. comprises four essential components: luciferase, luciferin, oxygen and calcium ion. For Friderica heliota, the luminescent reaction requires five components: luciferase, luciferin, ATP, magnesium ion and oxygen. Along with luciferin, more than a dozen analogues were isolated from worm biomass. These novel peptide-like natural compounds represent an unprecedented chemistry found in terrestrial organisms.


Assuntos
Luminescência , Oligoquetos/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Cálcio/metabolismo , Cor , Concentração de Íons de Hidrogênio , Luciferases/metabolismo , Proteínas Luminescentes/metabolismo , Magnésio/metabolismo , Oxigênio/metabolismo , Especificidade da Espécie , Temperatura
3.
Chemistry ; 21(10): 3942-7, 2015 Mar 02.
Artigo em Inglês | MEDLINE | ID: mdl-25650756

RESUMO

We report isolation and structure elucidation of AsLn5, AsLn7, AsLn11 and AsLn12: novel luciferin analogs from the bioluminescent earthworm Fridericia heliota. They were found to be highly unusual modified peptides, comprising either of the two tyrosine-derived chromophores, CompX or CompY and a set of amino acids, including threonine, gamma-aminobutyric acid, homoarginine, and unsymmetrical N,N-dimethylarginine. These natural compounds represent a unique peptide chemistry found in terrestrial animals and rise novel questions concerning their biosynthetic origin.


Assuntos
Luciferina de Vaga-Lumes/química , Substâncias Luminescentes/química , Oligoquetos/química , Peptídeos/química , Ácido gama-Aminobutírico/química , Animais , Arginina/análogos & derivados , Arginina/química , Espectroscopia de Ressonância Magnética
4.
Angew Chem Int Ed Engl ; 53(22): 5566-8, 2014 May 26.
Artigo em Inglês | MEDLINE | ID: mdl-24737705

RESUMO

The structure elucidation and synthesis of the luciferin from the recently discovered luminous earthworm Fridericia heliota is reported. This luciferin is a key component of a novel ATP-dependent bioluminescence system. UV, fluorescence, NMR, and HRMS spectroscopy studies were performed on 0.005 mg of the isolated substance and revealed four isomeric structures that conform to spectral data. These isomers were chemically synthesized and one of them was found to produce light when reacted with a protein extract from F. heliota. The novel luciferin was found to have an unusual extensively modified peptidic nature, thus implying an unprecedented mechanism of action.


Assuntos
Substâncias Luminescentes/química , Oligoquetos/metabolismo , Trifosfato de Adenosina/metabolismo , Animais , Isomerismo , Substâncias Luminescentes/síntese química , Medições Luminescentes , Peptídeos/química , Sibéria
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